TNFL6_HUMAN - dbPTM
TNFL6_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TNFL6_HUMAN
UniProt AC P48023
Protein Name Tumor necrosis factor ligand superfamily member 6
Gene Name FASLG
Organism Homo sapiens (Human).
Sequence Length 281
Subcellular Localization Cell membrane
Single-pass type II membrane protein . Cytoplasmic vesicle lumen . Lysosome lumen . Is internalized into multivesicular bodies of secretory lysosomes after phosphorylation by FGR and monoubiquitination (PubMed:17164290). Colocalizes w
Protein Description Cytokine that binds to TNFRSF6/FAS, a receptor that transduces the apoptotic signal into cells. [PubMed: 26334989]
Protein Sequence MQQPFNYPYPQIYWVDSSASSPWAPPGTVLPCPTSVPRRPGQRRPPPPPPPPPLPPPPPPPPLPPLPLPPLKKRGNHSTGLCLLVMFFMVLVALVGLGLGMFQLFHLQKELAELRESTSQMHTASSLEKQIGHPSPPPEKKELRKVAHLTGKSNSRSMPLEWEDTYGIVLLSGVKYKKGGLVINETGLYFVYSKVYFRGQSCNNLPLSHKVYMRNSKYPQDLVMMEGKMMSYCTTGQMWARSSYLGAVFNLTSADHLYVNVSELSLVNFEESQTFFGLYKL
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
82S-palmitoylationGNHSTGLCLLVMFFM
CCHHHHHHHHHHHHH
2.6721368861
135PhosphorylationEKQIGHPSPPPEKKE
HHHHCCCCCCCCHHH
44.3521964256
184N-linked_GlycosylationKKGGLVINETGLYFV
EECCEEECCCCCEEE
33.04UniProtKB CARBOHYD
184N-linked_GlycosylationKKGGLVINETGLYFV
EECCEEECCCCCEEE
33.049405425
208PhosphorylationSCNNLPLSHKVYMRN
CCCCCCCCCEEEECC
21.2323532336
212PhosphorylationLPLSHKVYMRNSKYP
CCCCCEEEECCCCCC
8.6523532336
231PhosphorylationMMEGKMMSYCTTGQM
EECCEEHHHCCHHHH
17.3523312004
232PhosphorylationMEGKMMSYCTTGQMW
ECCEEHHHCCHHHHH
3.9523312004
234PhosphorylationGKMMSYCTTGQMWAR
CEEHHHCCHHHHHHH
26.23-
250N-linked_GlycosylationSYLGAVFNLTSADHL
HHHHHHHCCCCCCEE
35.49UniProtKB CARBOHYD
250N-linked_GlycosylationSYLGAVFNLTSADHL
HHHHHHHCCCCCCEE
35.499405425
260N-linked_GlycosylationSADHLYVNVSELSLV
CCCEEEEEHHHEEEE
20.31UniProtKB CARBOHYD
260N-linked_GlycosylationSADHLYVNVSELSLV
CCCEEEEEHHHEEEE
20.319405425

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of TNFL6_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TNFL6_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of TNFL6_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TR10B_HUMANTNFRSF10Bphysical
15659383
TNR1A_HUMANTNFRSF1Aphysical
15659383
FADD_HUMANFADDphysical
12887920
CASP8_HUMANCASP8physical
12887920
TNR6_HUMANFASphysical
12887920
FNBP1_HUMANFNBP1physical
12023017
PACN2_HUMANPACSIN2physical
12023017
GRB2_HUMANGRB2physical
12023017
FINC_HUMANFN1physical
11276204
FYN_HUMANFYNphysical
11741599
GRB2_HUMANGRB2physical
11741599
LCK_HUMANLCKphysical
11741599
TNR1A_HUMANTNFRSF1Aphysical
12753742
TNR6_HUMANFASphysical
12753742
FADD_HUMANFADDphysical
12753742
CASP8_HUMANCASP8physical
12753742
LYN_HUMANLYNphysical
19807924
OSTF1_HUMANOSTF1physical
19807924
SNX33_HUMANSNX33physical
19807924
HCK_HUMANHCKphysical
19807924
NCK1_HUMANNCK1physical
19807924
YES_HUMANYES1physical
19807924
SRC_HUMANSRCphysical
19807924
SNX9_HUMANSNX9physical
19807924
SRGP1_HUMANSRGAP1physical
19807924
SPD2B_HUMANSH3PXD2Bphysical
19807924
BTK_HUMANBTKphysical
19807924
ES8L3_HUMANEPS8L3physical
19807924
RHG09_HUMANARHGAP9physical
19807924
MYO15_HUMANMYO15Aphysical
19807924
NCK2_HUMANNCK2physical
19807924
FYB1_HUMANFYBphysical
19807924
TEC_HUMANTECphysical
19807924
SPTA1_HUMANSPTA1physical
19807924
SAMN1_HUMANSAMSN1physical
19807924
SH3R2_HUMANSH3RF2physical
19807924
DLG2_HUMANDLG2physical
19807924
VINEX_HUMANSORBS3physical
19807924
SKAP2_HUMANSKAP2physical
19807924
CRK_HUMANCRKphysical
19807924
SPN90_HUMANNCKIPSDphysical
19807924
SPD2A_HUMANSH3PXD2Aphysical
19807924
BI2L1_HUMANBAIAP2L1physical
19807924
SH3G3_HUMANSH3GL3physical
19807924
ZO3_HUMANTJP3physical
19807924
CACB3_HUMANCACNB3physical
19807924
MPP4_HUMANMPP4physical
19807924
PK3CA_HUMANPIK3CAphysical
19807924
DNMBP_HUMANDNMBPphysical
19807924
DOCK4_HUMANDOCK4physical
19807924
KALRN_HUMANKALRNphysical
19807924
MACC1_HUMANMACC1physical
19807924
SRGP3_HUMANSRGAP3physical
19807924
FYN_HUMANFYNphysical
19807924
MIA_HUMANMIAphysical
19807924
SRGP2_HUMANSRGAP2physical
19807924
ITSN2_HUMANITSN2physical
19807924
NCF1_HUMANNCF1physical
19807924
ITK_HUMANITKphysical
19807924
CACB4_HUMANCACNB4physical
19807924
RIM3C_HUMANRIMBP3Cphysical
19807924
SNX18_HUMANSNX18physical
19807924
TNR6_HUMANFASphysical
21803845
FADD_HUMANFADDphysical
21803845
CFLAR_HUMANCFLARphysical
21803845
CASP8_HUMANCASP8physical
21803845
TRIP6_HUMANTRIP6physical
25416956
RGS20_HUMANRGS20physical
25416956
K1C40_HUMANKRT40physical
25416956
NT2NL_HUMANNOTCH2NLphysical
25416956
SNX9_HUMANSNX9physical
26186194
CLPX_HUMANCLPXphysical
26186194
SC65_HUMANP3H4physical
26186194
ANM2_HUMANPRMT2physical
26186194
SNX33_HUMANSNX33physical
26186194
E2AK1_HUMANEIF2AK1physical
26186194
P3H3_HUMANLEPREL2physical
26186194
MSPD2_HUMANMOSPD2physical
26186194
P85A_HUMANPIK3R1physical
25241761
FYN_HUMANFYNphysical
25241761
FINC_HUMANFN1physical
25241761
ANM2_HUMANPRMT2physical
28514442
E2AK1_HUMANEIF2AK1physical
28514442
SNX33_HUMANSNX33physical
28514442
MSPD2_HUMANMOSPD2physical
28514442
P3H3_HUMANLEPREL2physical
28514442

Drug and Disease Associations
Kegg Disease
H00108 Autoimmune lymphoproliferative syndromes (ALPS), including the following five diseases: CD95 (Fas) d
OMIM Disease
601859Autoimmune lymphoproliferative syndrome 1B (ALPS1B)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TNFL6_HUMAN

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Related Literatures of Post-Translational Modification

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